Results 1 to 10 of about 19,635 (271)

Roles of Anthrax Toxin Receptor 2 in Anthrax Toxin Membrane Insertion and Pore Formation [PDF]

open access: yesToxins, 2016
Interaction between bacterial toxins and cellular surface receptors is an important component of the host-pathogen interaction. Anthrax toxin protective antigen (PA) binds to the cell surface receptor, enters the cell through receptor-mediated ...
Jianjun Sun, Pedro Jacquez
doaj   +6 more sources

Tumor endothelium marker-8 based decoys exhibit superiority over capillary morphogenesis protein-2 based decoys as anthrax toxin inhibitors. [PDF]

open access: yesPLoS ONE, 2011
Anthrax toxin is the major virulence factor produced by Bacillus anthracis. The toxin consists of three protein subunits: protective antigen (PA), lethal factor, and edema factor.
Chenguang Cai   +8 more
doaj   +5 more sources

Evidence against a human cell-specific role for LRP6 in anthrax toxin entry. [PDF]

open access: yesPLoS ONE, 2008
The role of the cellular protein LRP6 in anthrax toxin entry is controversial. Previous studies showed that LRP6 was important for efficient intoxication of human M2182 prostate carcinoma cells but other studies performed with cells from gene-knockout ...
Patricia L Ryan, John A T Young
doaj   +5 more sources

Development of a New Cell-Based AP-1 Gene Reporter Potency Assay for Anti-Anthrax Toxin Therapeutics [PDF]

open access: yesToxins, 2023
Anthrax toxin is a critical virulence factor of Bacillus anthracis. The toxin comprises protective antigen (PA) and two enzymatic moieties, edema factor (EF) and lethal factor (LF), forming bipartite lethal toxin (LT) and edema toxin (ET).
Weiming Ouyang   +3 more
doaj   +2 more sources

Anthrax toxin translocation complex reveals insight into the lethal factor unfolding and refolding mechanism [PDF]

open access: yesScientific Reports, 2021
Translocation is essential to the anthrax toxin mechanism. Protective antigen (PA), the binding component of this AB toxin, forms an oligomeric pore that translocates lethal factor (LF) or edema factor, the active components of the toxin, into the cell ...
Alexandra J. Machen   +2 more
doaj   +2 more sources

Inhibitory Effects of a Reengineered Anthrax Toxin on Canine Oral Mucosal Melanomas [PDF]

open access: yesToxins, 2020
Canine oral mucosal melanomas (OMM) are the most common oral malignancy in dogs and few treatments are available. Thus, new treatment modalities are needed for this disease.
Adriana Tomoko Nishiya   +13 more
doaj   +2 more sources

Identification of Potential Therapeutic Targets Against Anthrax-Toxin-Induced Liver and Heart Damage [PDF]

open access: yesToxins
Anthrax represents a disease resulting from infection by toxin-secreting bacteria, Bacillus anthracis. This research aimed to identify new therapeutic targets to combat anthrax.
Lihong Wu   +10 more
doaj   +2 more sources

Anthrax toxin uptake by primary immune cells as determined with a lethal factor-beta-lactamase fusion protein. [PDF]

open access: yesPLoS ONE, 2009
BACKGROUND:To initiate infection, Bacillus anthracis needs to overcome the host innate immune system. Anthrax toxin, a major virulence factor of B. anthracis, impairs both the innate and adaptive immune systems and is important in the establishment of ...
Haijing Hu, Stephen H Leppla
doaj   +5 more sources

Disulfide bonds in the ectodomain of anthrax toxin receptor 2 are required for the receptor-bound protective-antigen pore to function. [PDF]

open access: yesPLoS ONE, 2010
Cell-surface receptors play essential roles in anthrax toxin action by providing the toxin with a high-affinity anchor and self-assembly site on the plasma membrane, mediating the toxin entry into cells through endocytosis, and shifting the pH threshold ...
Jianjun Sun, R John Collier
doaj   +5 more sources

Lack of evidence for a role of anthrax toxin receptors as surface receptors for collagen VI and for its cleaved-off C5 domain/endotrophin [PDF]

open access: yesiScience, 2022
Summary: The microfibril-forming collagen VI is proteolytically cleaved and it was proposed that the released C-terminal Kunitz domain (C5) of the α3 chain is an adipokine important for tumor progression and fibrosis.
Matthias Przyklenk   +8 more
doaj   +2 more sources

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